The flavoprotein SoxF functions in chemotrophic thiosulfate oxidation of Paracoccus pantotrophus in vivo and in vitro

FEMS Microbiology Letters
Frank BardischewskyC G Friedrich

Abstract

Paracoccus pantotrophus strain GBsoxFDelta carries a deletion in the soxF gene that inactivates flavoprotein SoxF-sulfide dehydrogenase. This strain grew with thiosulfate slower than the wild type. GBsoxFDelta cells oxidized thiosulfate at a rate of 40% and hydrogen sulfide at a rate of 45% of the wild type. Complementation of GBsoxFDelta with plasmid pRIsoxF carrying the soxF gene increased these rates to 83% and 70%, respectively. However, GBsoxFDelta and GBsoxFDelta (pRIsoxF) oxidized thiosulfate and hydrogen sulfide to sulfate as evident from the yield of electrons. The thiosulfate oxidation rate of cell-free extracts of strain GBsoxFDelta was increased when supplemented with SoxF isolated from the wild type. However, SoxF did not affect the thiosulfate-oxidizing activity of the Sox enzyme system as reconstituted from the 'as-isolated' four Sox proteins. These data demonstrated that SoxF enhanced chemotrophic thiosulfate oxidation in vivo and acted on some component or condition present in whole cells and cell-free extracts but not present in the reconstituted system.

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Citations

Feb 10, 2010·Photosynthesis Research·Hidehiro SakuraiKazuhito Inoue
May 26, 2009·Applied and Environmental Microbiology·Sabrina SchübbeDennis A Bazylinski
Aug 22, 2012·Cellular and Molecular Life Sciences : CMLS·Ulrike Kappler, Megan J Maher
Dec 15, 2015·Proceedings of the National Academy of Sciences of the United States of America·Daniel B GrabarczykBen C Berks
Nov 26, 2008·Journal of Bacteriology·Leong-Keat ChanThomas E Hanson

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